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Database: UniProt/TrEMBL
Entry: M4NDA3_9GAMM
LinkDB: M4NDA3_9GAMM
Original site: M4NDA3_9GAMM 
ID   M4NDA3_9GAMM            Unreviewed;       328 AA.
AC   M4NDA3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-SEP-2017, entry version 36.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369716};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369716};
DE   Flags: Precursor;
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   ORFNames=R2APBS1_1541 {ECO:0000313|EMBL:AGG88684.1};
OS   Rhodanobacter denitrificans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=666685 {ECO:0000313|EMBL:AGG88684.1, ECO:0000313|Proteomes:UP000011859};
RN   [1] {ECO:0000313|EMBL:AGG88684.1, ECO:0000313|Proteomes:UP000011859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2APBS1 {ECO:0000313|EMBL:AGG88684.1,
RC   ECO:0000313|Proteomes:UP000011859};
RG   US DOE Joint Genome Institute;
RA   Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Munk A.C.C., Chen A., Krypides N., Mavromatis K., Markowitz V.,
RA   Szeto E., Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I.,
RA   Pati A., Goodwin L., Peters L., Pitluck S., Woyke T., Prakash O.,
RA   Elkins J., Brown S., Palumbo A., Hemme C., Zhou J., Watson D.,
RA   Jardine P., Kostka J., Green S.;
RT   "Complete genome of Rhodanobacter sp. 2APBS1.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {ECO:0000256|HAMAP-Rule:MF_01517,
CC       ECO:0000256|SAAS:SAAS00755561}.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC       {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369698}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01517}.
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DR   EMBL; CP003470; AGG88684.1; -; Genomic_DNA.
DR   RefSeq; WP_015447465.1; NC_020541.1.
DR   EnsemblBacteria; AGG88684; AGG88684; R2APBS1_1541.
DR   GeneID; 31836054; -.
DR   KEGG; rhd:R2APBS1_1541; -.
DR   KO; K00024; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000011859; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01517; Malate_dehydrog_2; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR23382; PTHR23382; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000011859};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   DOMAIN        5    149       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      157    319       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      11     17       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   NP_BIND     129    131       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      92     92       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING      98     98       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     105    105       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     112    112       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     131    131       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
SQ   SEQUENCE   328 AA;  34859 MW;  617F9A4AC49D503B CRC64;
     MKAPVRVAVT GAAGQIGYAL LFRIAAGDML GPDQPVILHL LEITPALPSL QGVVMELNDC
     AFPTLAGVVA TDDANVAFKD VDYALLVGAR PRGPGMERKD LLEANGAIFG PQGKALNAHA
     KRGVRVLVVG NPANTNALIA QQNAPDLDPK CFTAMVRLDH NRAKSQLAEK TGKHNTDVKK
     MTIWGNHSST QYPDLHHASV DGKSALSLVD QAWYESDFIP TVQQRGAAII KARGASSAAS
     AASAAIDHMR TWALGTAEGD WVSMGIPSDG SYGIAPGVIY GYPVTVKNGQ YAIVQGLEIN
     AFSRARMDAT DKELREERAG VEHLFAKK
//
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